Affinage

LITAF

Lipopolysaccharide-induced tumor necrosis factor-alpha factor · UniProt Q99732

Length
161 aa
Mass
17.1 kDa
Annotated
2026-06-10
100 papers in source corpus 15 papers cited in narrative 15 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

LITAF (also SIMPLE/PIG7) is a zinc-binding monotopic membrane protein that integrates innate-immune and trafficking functions at the endolysosomal system (PMID:27582497). Biochemically, it associates with membranes through a single hydrophobic region without translocating either terminus into the ER lumen, both N- and C-termini facing the cytoplasm, and binds one mole of zinc whose coordinating residues are required for membrane association (PMID:27582497). Its conserved C-terminal LITAF domain is necessary and sufficient to target the protein to the late endosome/lysosome via the secretory pathway (PMID:25058650). In macrophages, LITAF acts as an inflammatory effector downstream of TLR2/TLR4–MyD88 signaling, where it is phosphorylated by p38α (and controlled by ERK2) to drive nuclear translocation and expression of TNF-α and other cytokines, distinct from the NF-κB pathway; loss of LITAF reduces cytokine output and protects against LPS lethality and TNBS colitis (PMID:16954198, PMID:26918116, PMID:21984950). LITAF also operates as a transcriptional node in other contexts, acting downstream of AMPK to bind the TNFSF15 promoter and restrain tumor growth, and being repressed by BCL6 in B cells where it instead supports starvation-induced autophagy (PMID:21217782, PMID:23795761). Through two N-terminal PPXY motifs it binds the ubiquitin ligase Itch and redirects it from the trans-Golgi network to lysosomes, linking LITAF to endolysosomal ubiquitin-dependent trafficking (PMID:21326863). Independently, LITAF serves as a host cell-surface receptor for the Bacillus cereus pore-forming toxin hemolysin BL, with CDIP1 acting as an alternative receptor (PMID:32544461). Missense mutations clustered in a five-residue stretch of the C-terminal domain (e.g. G112S, T115N, W116G) cause autosomal-dominant demyelinating Charcot-Marie-Tooth disease type 1C by mislocalizing the protein from lysosomes to mitochondria, dominantly redirecting wild-type LITAF and disrupting Schwann-cell function (PMID:12525712, PMID:25058650, PMID:15122712).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2001 Medium

    Established the basic identity of LITAF/SIMPLE as a small, unglycosylated integral membrane protein of the late endosome/lysosome rather than a RING-type or nuclear protein, correcting the initial sequence-based assumption.

    Evidence cDNA cloning, genome analysis, and cell-fractionation/localization experiments in monocytes

    PMID:11274176

    Open questions at the time
    • Membrane topology and metal-binding not resolved
    • No defined molecular activity assigned
  2. 2003 High

    Demonstrated that LITAF mutations cause human disease by mapping CMT1C to a tight cluster of missense mutations in the C-terminal domain, defining a region critical for peripheral nerve function.

    Evidence Positional/candidate cloning and mutation screening in CMT1C pedigrees with Western/Northern blots

    PMID:12525712

    Open questions at the time
    • Cellular mechanism by which mutations impair myelination unknown
    • No demonstration of where mutant protein mislocalizes
  3. 2004 Medium

    Tied the genetic disease to the affected cell type by showing SIMPLE/LITAF is expressed in Schwann cells and that demyelinating mutations cluster in a five-residue domain.

    Evidence Large-cohort mutation screening, haplotype/electrophysiology, sciatic nerve immunohistochemistry

    PMID:15122712

    Open questions at the time
    • Molecular consequence of mutations still undefined
    • Schwann-cell function of wild-type LITAF unknown
  4. 2006 High

    Placed LITAF in a specific innate-immune signaling pathway, showing it acts as a transcription factor downstream of TLR/MyD88 and is phosphorylated by p38α to translocate to the nucleus and drive cytokine expression, separate from NF-κB.

    Evidence Macrophage-specific knockout mice, kinase array, p38α inhibition, TLR-knockout macrophages, cDNA rescue, in vivo LPS challenge

    PMID:16954198

    Open questions at the time
    • How a membrane-anchored protein reaches the nucleus mechanistically unresolved
    • Direct DNA target sites in cytokine genes not defined here
  5. 2011 Medium

    Connected LITAF to ubiquitin-dependent trafficking by identifying a PPXY-mediated interaction with the ligase Itch and showing LITAF recruits Itch from the TGN to lysosomes.

    Evidence Reciprocal co-immunoprecipitation, immunofluorescence, and PPXY motif mutagenesis in multiple cell lines

    PMID:21326863

    Open questions at the time
    • Functional consequence of Itch relocalization (substrates) not defined
    • Single lab, no in vivo validation
  6. 2011 Medium

    Defined an AMPK–LITAF–TNFSF15 transcriptional axis and a tumor-suppressor role, showing LITAF is induced by AMPK and binds the TNFSF15 promoter to limit cancer-cell growth.

    Evidence shRNA knockdown, dominant-negative AMPK, AICAR, promoter binding assay, prostate xenograft and growth assays

    PMID:21217782

    Open questions at the time
    • How a lysosomal membrane protein engages a promoter not reconciled
    • Single lab
  7. 2011 Medium

    Extended the macrophage TNF-α role to intestinal disease, showing LITAF drives lamina propria macrophage TNF-α secretion during colitis.

    Evidence TNBS colitis model with macrophage-specific LITAF knockout mice, ex vivo LPM TNF-α secretion and MPO assays

    PMID:21984950

    Open questions at the time
    • Upstream sensing in this tissue not dissected
    • Single lab
  8. 2013 Medium

    Revealed context-dependent regulation and a distinct cellular function, showing BCL6 represses LITAF in B cells where LITAF promotes autophagy rather than TNF secretion.

    Evidence ChIP, luciferase reporter, BCL6 silencing, gain/loss-of-function in B-cell lymphoma lines, autophagosome co-localization

    PMID:23795761

    Open questions at the time
    • Molecular basis of autophagy regulation by LITAF unknown
    • Why TNF induction is absent in B cells unexplained
  9. 2014 Medium

    Provided the cell-biological mechanism of CMT1C by showing disease mutations mislocalize LITAF from lysosomes to mitochondria, that the C-terminus is necessary and sufficient for lysosomal targeting, and that mutants dominantly redirect wild-type protein.

    Evidence Immunofluorescence localization of multiple mutants, Brefeldin A secretory-pathway block, C-terminal truncations, WT/mutant co-transfection

    PMID:25058650

    Open questions at the time
    • How mitochondrial mislocalization damages Schwann cells unresolved
    • Single lab, transfected-cell system
  10. 2014 Medium

    Linked a LITAF variant to a trafficking phenotype relevant to peripheral neuropathy, showing I92V partially mislocalizes to mitochondria and promotes PMP22 accumulation.

    Evidence Transfection/immunofluorescence of I92V, PMP22 accumulation assay, clinical cohort analysis

    PMID:25342198

    Open questions at the time
    • Mechanism linking LITAF mislocalization to PMP22 handling unclear
    • Single lab
  11. 2015 Medium

    Refined the macrophage signaling module by identifying ERK2 (via Ser206) as an upstream kinase controlling LITAF nuclear translocation and LPS-induced TNF-α.

    Evidence LITAF-/- and ERK2-/- macrophages with ERK2 rescue, ERK2 S206 analysis, in vivo CAIA arthritis model

    PMID:26918116

    Open questions at the time
    • Relationship between ERK2 and p38α inputs not integrated
    • Direct phosphosite on LITAF not mapped
  12. 2016 High

    Resolved the long-standing topology and metal-binding questions, establishing LITAF as a zinc-binding monotopic membrane protein with both termini cytoplasmic, sharing topology with CDIP1.

    Evidence In vitro translation/microsome integration, glycosylation reporters, immunofluorescence latency assay, ICP-MS zinc measurement, zinc-residue mutagenesis

    PMID:27582497

    Open questions at the time
    • Functional role of zinc binding beyond membrane association unknown
    • How cytoplasmic-facing topology permits nuclear/transcriptional roles unexplained
  13. 2018 Medium

    Placed LITAF in DNA-damage signaling, showing it is a direct miR-106a target and mediates ATM upregulation and radiosensitivity in prostate cancer cells.

    Evidence 3'UTR luciferase assay, western blotting, miR-106a/LITAF perturbation, radiation resistance and transcriptomic analysis

    PMID:29845714

    Open questions at the time
    • Mechanistic link between LITAF and ATM not biochemically defined
    • Single lab
  14. 2019 Low

    Proposed an additional radiosensitization function in glioma via the FoxO1 pathway and apoptotic effectors.

    Evidence LITAF knockdown/overexpression in glioma lines, radiation and apoptosis assays, FoxO1 pathway analysis

    PMID:31098771

    Open questions at the time
    • No direct biochemical interaction between LITAF and FoxO1 shown
    • Single cell-line system, single lab
  15. 2020 High

    Identified a wholly distinct function as a toxin receptor, showing LITAF (and alternatively CDIP1) is the host membrane receptor for Bacillus cereus hemolysin BL, with LITAF-deficient cells and mice resistant to the toxin.

    Evidence Two sequential genome-wide CRISPR-Cas9 knockout screens, LITAF-deficient cells and mice, in vivo HBL lethality challenge

    PMID:32544461

    Open questions at the time
    • Direct toxin-LITAF binding interface not defined
    • Relationship between receptor role and endolysosomal/transcriptional functions unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how a zinc-binding, cytoplasmic-facing monotopic endolysosomal membrane protein executes its reported nuclear transcription-factor activities, and how its trafficking, immune, autophagy, and toxin-receptor roles are mechanistically unified.
  • No structure of LITAF or its complexes
  • No mechanism for membrane-to-nucleus relocation
  • No unified model linking the functional contexts

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140110 transcription regulator activity 2 GO:0001618 virus receptor activity 1 GO:0003677 DNA binding 1 GO:0008289 lipid binding 1
Localization
GO:0005764 lysosome 3 GO:0005768 endosome 3 GO:0005634 nucleus 2 GO:0005739 mitochondrion 2 GO:0005886 plasma membrane 1
Pathway
R-HSA-1643685 Disease 3 R-HSA-168256 Immune System 3 R-HSA-74160 Gene expression (Transcription) 3 R-HSA-9612973 Autophagy 1
Partners
CDIP1ITCH

Evidence

Reading pass · 15 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2006 LITAF functions as a transcription factor mediating LPS-induced cytokine (TNF-α, IL-6, sTNF-RII, CXCL16) expression in macrophages. p38α kinase was identified as the specific kinase that phosphorylates LITAF and mediates its nuclear translocation; inhibition of p38α with SB203580 blocked LITAF nuclear translocation and reduced LPS-induced TNF-α. The LITAF pathway is downstream of TLR-2 and TLR-4 (both requiring MyD88) and is distinct from the NF-κB pathway. Macrophage-specific LITAF-knockout mice showed reduced cytokine levels and increased resistance to LPS-induced lethality. Macrophage-specific knockout mouse, kinase array, p38α inhibitor (SB203580), TLR2/4/9 knockout macrophages, LITAF cDNA rescue transfection, in vivo LPS challenge Proceedings of the National Academy of Sciences of the United States of America High 16954198
2001 LITAF/PIG7 and the newly identified SIMPLE protein are small integral membrane proteins of the lysosome/late endosome. Experimental evidence (including detailed analysis of domain structure) showed the protein is neither a RING family member nor a nuclear protein, despite possessing a RING domain signature. The protein is unglycosylated and its expression in monocytes is induced by BCG, LPS, and TNF-α. Differential display cloning, full-length cDNA cloning, expressed sequence tag search, genome sequence analysis, cell fractionation/localization experiments The Journal of biological chemistry Medium 11274176
2003 Missense mutations G112S, T115N, and W116G in LITAF/SIMPLE cause CMT type 1C (autosomal dominant demyelinating neuropathy). The mutations cluster within a small domain of the LITAF protein, defining a region critical for peripheral nerve function. Western blot showed T115N and W116G mutations do not alter LITAF protein levels. Positional cloning, candidate gene approach, Western blot, Northern blot, mutation screening in CMT1C pedigrees Neurology High 12525712
2011 LITAF interacts with the WW-domain-containing ubiquitin ligase Itch via two PPXY motifs in the N-terminus of LITAF. Co-expression of LITAF with Itch relocates Itch from the trans-Golgi network to lysosomes. LITAF itself localizes to the late endosome/lysosomal compartment. Disruption of the PPXY motifs abrogates Itch re-localization. Co-immunoprecipitation, immunofluorescence, subcellular localization in multiple cell lines, PPXY motif mutagenesis PloS one Medium 21326863
2011 LITAF is a downstream transcriptional target of AMPK. AMPK activation upregulates LITAF transcription, and LITAF binds to a specific sequence in the promoter region of TNFSF15 to regulate its transcription. Silencing LITAF by shRNA enhances proliferation and anchorage-independent growth of prostate cancer cells, suggesting a tumor suppressor function. This establishes an AMPK–LITAF–TNFSF15 regulatory axis. shRNA knockdown, dominant-negative AMPK mutant, AMPK activator (AICAR), promoter binding assay, xenograft tumor model, in vitro proliferation/anchorage-independent growth assays Oncogene Medium 21217782
2013 BCL6 directly represses LITAF transcription in B cells. LITAF does not induce LPS-mediated TNF secretion in B cells (negative result in this cellular context). Instead, LITAF regulates autophagy in B-cell lymphomas: ectopic LITAF expression enhances autophagy in response to starvation, while LITAF silencing impairs it. LITAF co-localizes with autophagosomes in B cells. Chromatin immunoprecipitation (ChIP), luciferase reporter assay, BCL6 silencing, gain- and loss-of-function in B-cell lymphoma lines, gene expression microarrays, immunofluorescence co-localization British journal of haematology Medium 23795761
2014 CMT1C-associated LITAF mutations (A111G, G112S, W116G, T115N) cause mislocalization of LITAF from the late endosome/lysosome to the mitochondria. Mutations T49M, L122V, and P135T show partial mislocalization. CMT1C mutants act in a dominant manner: co-transfection of wild-type LITAF with G112S or T49M mutants relocates wild-type LITAF to the mitochondria. Wild-type LITAF traffics to the late endosome/lysosome via the secretory pathway (blocked by Brefeldin A), whereas LITAF mutants transit to mitochondria independently of the secretory pathway. The C-terminus of LITAF is necessary and sufficient for late endosome/lysosome targeting. Subcellular localization by immunofluorescence in transfected cells, Brefeldin A treatment, C-terminal truncation constructs, co-transfection of WT and mutant LITAF PloS one Medium 25058650
2016 LITAF is a zinc-binding monotopic membrane protein. In vitro translation shows LITAF integrates poorly into ER-derived microsomes compared with the bona fide tail-anchored protein Sec61β. N-linked glycosylation reporters confirm that neither the N-terminal nor C-terminal domains of LITAF translocate into the ER lumen. Both N- and C-termini face the cytoplasm (immunofluorescence latency assay). Recombinant LITAF contains 1 mol/mol zinc; mutation of predicted zinc-binding residues disrupts LITAF membrane association. The related protein CDIP1 displays identical membrane topology. In vitro translation/microsome integration assay, glycosylation reporter constructs, immunofluorescence latency assay, zinc content measurement by ICP-MS, zinc-binding residue mutagenesis The Biochemical journal High 27582497
2015 ERK2 is the kinase upstream of LITAF that controls LPS-induced TNF-α expression. Kavain reduces LPS-induced TNF-α by dephosphorylating ERK2, which in turn prevents LITAF nuclear translocation. LITAF nuclear translocation depends on ERK2 Serine 206 residue. This effect was abrogated in both LITAF-/- and ERK2-/- macrophages. LITAF-knockout and ERK2-knockout primary macrophages, ERK2 gene re-introduction (rescue), site-directed analysis of ERK2 S206, in vivo CAIA arthritis model Toxicology research Medium 26918116
2011 LITAF mediates increased TNF-α secretion from lamina propria macrophages during colonic inflammation. Macrophage-specific LITAF knockout mice show reduced MPO activity and reduced colonic TNF-α mRNA following TNBS-induced colitis, and LITAF-deficient LPM secrete significantly less TNF-α in response to LPS. TNBS colitis mouse model, macrophage-specific LITAF knockout mice, LPM isolation, ex vivo TNF-α secretion assay, MPO activity assay, LITAF mRNA/protein measurement PloS one Medium 21984950
2020 LITAF functions as a host cell-surface or membrane receptor for the Bacillus cereus pore-forming toxin hemolysin BL (HBL). LITAF-deficient cells identified by genome-wide CRISPR-Cas9 knockout screen are resistant to HBL. A second CRISPR screen in LITAF-deficient cells identified CDIP1 as an alternative HBL receptor. LITAF-deficient mice exhibit marked resistance to lethal HBL challenges in vivo. Genome-wide CRISPR-Cas9 knockout screen (two sequential screens), LITAF-deficient cell lines, LITAF-deficient mouse generation, in vivo HBL lethality challenge Cell host & microbe High 32544461
2018 LITAF is a direct target of miR-106a (validated by 3'UTR luciferase assay and western blotting). LITAF knockdown phenocopies miR-106a overexpression in conferring radioresistance. LITAF mediates upregulation of ATM expression, providing a novel mechanistic link between LITAF and the DNA damage response in prostate cancer cells. 3'UTR luciferase reporter assay, western blotting, miR-106a overexpression and knockdown of LITAF, radiation resistance assays, transcriptomic analysis Molecular oncology Medium 29845714
2014 The LITAF I92V sequence variant partially mislocalizes to the mitochondria (compared to wild-type LITAF which localizes to late endosome/lysosomes) and is associated with a tendency for PMP22 to accumulate in cells. This variant predisposes CMT1A/HNPP patients to an earlier age of disease onset. Cell transfection with LITAF I92V construct, immunofluorescence-based subcellular localization, PMP22 accumulation assay, clinical cohort analysis Neurogenetics Medium 25342198
2004 LITAF/SIMPLE mutations (G112S, W116G, and others) are found exclusively in CMT1 (demyelinating) patients. SIMPLE protein is expressed in Schwann cells, the affected cell type in CMT1C. Clustering of mutations G112S, T115N, W116G within five amino acids identifies a critical domain for peripheral nerve myelination. Mutation screening of 152 neuropathy probands, haplotype analysis, electrophysiological studies, immunohistochemistry of sciatic nerve sections Annals of neurology Medium 15122712
2019 LITAF enhances radiosensitivity of glioma cells via the FoxO1 pathway and its downstream targets BIM, TRAIL, and FASLG. Knockdown or overexpression of LITAF did not affect proliferation or apoptosis under basal conditions, but modulated radiation response through FoxO1. LITAF knockdown and overexpression in glioma cell lines, radiation assays, FoxO1 pathway analysis, apoptosis assays Cellular and molecular neurobiology Low 31098771

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1990 Rapid and simple method for purification of nucleic acids. Journal of clinical microbiology 3873 1691208
2006 Notch signalling: a simple pathway becomes complex. Nature reviews. Molecular cell biology 2108 16921404
1992 Slippage synthesis of simple sequence DNA. Nucleic acids research 667 1741246
2018 Biased signalling: from simple switches to allosteric microprocessors. Nature reviews. Drug discovery 603 29302067
2004 The complex life of simple sphingolipids. EMBO reports 526 15289826
2014 Absence of a simple code: how transcription factors read the genome. Trends in biochemical sciences 388 25129887
2006 Simple sequence repeats as advantageous mutators in evolution. Trends in genetics : TIG 371 16567018
2021 A simple method for quantitating confocal fluorescent images. Biochemistry and biophysics reports 356 33553685
2014 Ceramide: a simple sphingolipid with unique biophysical properties. Progress in lipid research 316 24513486
2004 Gaucher disease: complexity in a "simple" disorder. Molecular genetics and metabolism 314 15464415
2008 Sister chromatid cohesion: a simple concept with a complex reality. Annual review of cell and developmental biology 267 18616427
2017 Serum Creatinine: Not So Simple! Nephron 242 28441651
2004 T-cell development made simple. Nature reviews. Immunology 213 14704769
2013 Ethylene signaling: simple ligand, complex regulation. Current opinion in plant biology 182 24012247
1994 Simple sequences. Current opinion in genetics & development 177 7888752
2005 Intracellular glucocorticoid signaling: a formerly simple system turns stochastic. Science's STKE : signal transduction knowledge environment 176 16204701
2007 Physiological polyamines: simple primordial stress molecules. Journal of cellular and molecular medicine 164 17760833
2019 Pyruvate kinase M2: A simple molecule with complex functions. Free radical biology & medicine 154 31401304
2006 LPS-induced TNF-alpha factor (LITAF)-deficient mice express reduced LPS-induced cytokine: Evidence for LITAF-dependent LPS signaling pathways. Proceedings of the National Academy of Sciences of the United States of America 153 16954198
2013 PTP1B: a simple enzyme for a complex world. Critical reviews in biochemistry and molecular biology 148 23879520
2010 Endocannabinoid biosynthesis and inactivation, from simple to complex. Drug discovery today 148 20304091
2003 Mutation of a putative protein degradation gene LITAF/SIMPLE in Charcot-Marie-Tooth disease 1C. Neurology 141 12525712
2009 Dscam and DSCAM: complex genes in simple animals, complex animals yet simple genes. Genes & development 136 19171779
2010 Social interactions in "simple" model systems. Neuron 128 20346755
1997 Calcineurin: not just a simple protein phosphatase. Biochemical and biophysical research communications 127 9199180
1991 Cyclins and their partners: from a simple idea to complicated reality. Seminars in cell biology 120 1842340
2005 Quasispecies made simple. PLoS computational biology 115 16322763
2009 Filopodia: Complex models for simple rods. The international journal of biochemistry & cell biology 113 19433307
2001 Desiccation tolerance: a simple process? Trends in microbiology 112 11825716
2015 Protein detection by Simple Western™ analysis. Methods in molecular biology (Clifton, N.J.) 107 26044028
2006 Molecular cloning and characterization of chicken lipopolysaccharide-induced TNF-alpha factor (LITAF). Developmental and comparative immunology 100 16466659
2001 Mycobacterium bovis Bacillus Calmette-Guerin and its cell wall complex induce a novel lysosomal membrane protein, SIMPLE, that bridges the missing link between lipopolysaccharide and p53-inducible gene, LITAF(PIG7), and estrogen-inducible gene, EET-1. The Journal of biological chemistry 86 11274176
1985 Simple- and complex-cell response dependences on stimulation parameters. Journal of neurophysiology 83 3998808
2008 Neurobiology of a simple memory. Journal of neurophysiology 82 18463176
2013 SIRT3: as simple as it seems? Gerontology 80 24192814
2010 Simple is good: yeast models of neurodegeneration. FEMS yeast research 75 20579105
2018 Simple yet functional phosphate-loop proteins. Proceedings of the National Academy of Sciences of the United States of America 73 30504143
2015 Phenylbutyric Acid: simple structure - multiple effects. Current pharmaceutical design 69 25557635
2013 Two-partner secretion: as simple as it sounds? Research in microbiology 65 23542425
2011 LITAF and TNFSF15, two downstream targets of AMPK, exert inhibitory effects on tumor growth. Oncogene 65 21217782
2021 Human plasma IgG1 repertoires are simple, unique, and dynamic. Cell systems 62 34613904
2020 6-Hydroxydopamine: a far from simple neurotoxin. Journal of neural transmission (Vienna, Austria : 1996) 62 31894418
2006 Type IA topoisomerases: a simple puzzle? Biochimie 62 17141394
2017 Poliovirus Receptor: More than a simple viral receptor. Virus research 60 28870470
2018 Antisense oligonucleotides and other genetic therapies made simple. Practical neurology 56 29455156
2004 Grb10: more than a simple adaptor protein. Frontiers in bioscience : a journal and virtual library 55 14766376
2004 SIMPLE mutation in demyelinating neuropathy and distribution in sciatic nerve. Annals of neurology 54 15122712
2022 Anticancer peptides mechanisms, simple and complex. Chemico-biological interactions 53 36195187
2010 Simple genomes, complex interactions: epistasis in RNA virus. Chaos (Woodbury, N.Y.) 53 20590335
2019 Research Techniques Made Simple: Profiling the Skin Microbiota. The Journal of investigative dermatology 52 30904077
2008 Rituximab: beyond simple B cell depletion. Clinical reviews in allergy & immunology 52 18240027
2008 Identification and characterization of a putative lipopolysaccharide-induced TNF-alpha factor (LITAF) homolog from Singapore grouper iridovirus. Biochemical and biophysical research communications 52 18554501
2002 Detecting cryptically simple protein sequences using the SIMPLE algorithm. Bioinformatics (Oxford, England) 52 12050063
2013 DNA vaccines: a simple DNA sensing matter? Human vaccines & immunotherapeutics 43 23912600
2018 miRNA-106a and prostate cancer radioresistance: a novel role for LITAF in ATM regulation. Molecular oncology 42 29845714
2018 The genetics of aniridia - simple things become complicated. Journal of applied genetics 40 29460221
2008 Simple sequence repeats in Haemophilus influenzae. Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases 40 19095084
2013 LITAF, a BCL6 target gene, regulates autophagy in mature B-cell lymphomas. British journal of haematology 38 23795761
2021 Rotavirus cell entry: not so simple after all. Current opinion in virology 37 33887683
2014 How simple are 'simple renal cysts'? Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association 37 25165175
2001 Not as simple as just punching a hole. Toxicon : official journal of the International Society on Toxinology 36 11595627
2017 Bioengineering Hearts: Simple yet Complex. Current stem cell reports 35 28261549
2017 Precarious maintenance of simple DNA repeats in eukaryotes. BioEssays : news and reviews in molecular, cellular and developmental biology 35 28703879
2017 Dead simple OWL design patterns. Journal of biomedical semantics 33 28583177
2003 Interpreting enzyme and receptor kinetics: keeping it simple, but not too simple. Nuclear medicine and biology 32 14698785
1997 DNA topology: topoisomerases keep it simple. Current biology : CB 32 9382831
2007 Golgi biogenesis in simple eukaryotes. Cellular microbiology 31 17223925
1997 On simple repetitive DNA sequences and complex diseases. Electrophoresis 31 9378125
2022 Research Techniques Made Simple: Spatial Transcriptomics. The Journal of investigative dermatology 30 35331388
2020 Complexity of seemingly simple lipid nanodiscs. Biochimica et biophysica acta. Biomembranes 29 32712188
2011 SIMPLE/LITAF expression induces the translocation of the ubiquitin ligase itch towards the lysosomal compartments. PloS one 28 21326863
2010 Volvox: simple steps to developmental complexity? Current opinion in plant biology 27 21075047
2021 Chemical Diversification of Simple Synthetic Antibodies. ACS chemical biology 25 33482061
2021 Tetrahymena meiosis: Simple yet ingenious. PLoS genetics 25 34264933
2020 Sequential CRISPR-Based Screens Identify LITAF and CDIP1 as the Bacillus cereus Hemolysin BL Toxin Host Receptors. Cell host & microbe 25 32544461
2020 Simple transformations capture auditory input to cortex. Proceedings of the National Academy of Sciences of the United States of America 25 33097665
2017 Primordial membranes: more than simple container boundaries. Current opinion in chemical biology 25 28802999
2014 Rcount: simple and flexible RNA-Seq read counting. Bioinformatics (Oxford, England) 25 25322836
2011 LITAF mediation of increased TNF-α secretion from inflamed colonic lamina propria macrophages. PloS one 25 21984950
2021 Why have aggregative multicellular organisms stayed simple? Current genetics 24 34114051
2018 Cohesin mutations in myeloid malignancies made simple. Current opinion in hematology 24 29278534
2020 Cell intercalation in a simple epithelium. Philosophical transactions of the Royal Society of London. Series B, Biological sciences 23 32829682
2012 Characteristics and expression patterns of the lipopolysaccharide-induced TNF-α factor (LITAF) gene family in the Pacific oyster, Crassostrea gigas. Fish & shellfish immunology 22 22902610
1999 Cyclic adducts and intermediates induced by simple epoxides. IARC scientific publications 22 10626214
1998 A simple molecular model of neurulation. BioEssays : news and reviews in molecular, cellular and developmental biology 22 9819565
2014 LITAF mutations associated with Charcot-Marie-Tooth disease 1C show mislocalization from the late endosome/lysosome to the mitochondria. PloS one 21 25058650
2013 Characterization of LPS-induced TNFα factor (LITAF) from orange-spotted grouper, Epinephelus coioides. Fish & shellfish immunology 21 24091064
2021 Beyond GWAS: from simple associations to functional insights. Seminars in immunopathology 20 34605948
2012 Identification and characterization of a putative lipopolysaccharide-induced TNF-α factor (LITAF) gene from Amphioxus (Branchiostoma belcheri): an insight into the innate immunity of Amphioxus and the evolution of LITAF. Fish & shellfish immunology 20 22484607
2020 Simple Repeats as Building Blocks for Genetic Computers. Trends in genetics : TIG 19 32690316
2019 LITAF Enhances Radiosensitivity of Human Glioma Cells via the FoxO1 Pathway. Cellular and molecular neurobiology 19 31098771
2017 Simple limbal epithelial transplantation. Current opinion in ophthalmology 19 28406800
2011 The proteome of Mycoplasma pneumoniae, a supposedly "simple" cell. Proteomics 19 21751371
1997 CCR: a rapid and simple approach for mutation detection. Nucleic acids research 19 9207051
2022 Thulium fiber laser in urology: physics made simple. Current opinion in urology 18 34954703
2016 The Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic membrane protein. The Biochemical journal 18 27582497
2015 Kavain Inhibition of LPS-Induced TNF-α via ERK/LITAF. Toxicology research 18 26918116
2014 The LITAF/SIMPLE I92V sequence variant results in an earlier age of onset of CMT1A/HNPP diseases. Neurogenetics 18 25342198
2022 BUB3, beyond the Simple Role of Partner. Pharmaceutics 17 35631670
2014 A novel LITAF/SIMPLE mutation within a family with a demyelinating form of Charcot-Marie-Tooth disease. Journal of the neurological sciences 17 24880540

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